BMRB Entry 27636

Name: Thioredoxin-huntingtin exon 1(Q7) fusion
Published: 2018-11-14

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27636

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Thioredoxin-huntingtin exon 1(Q7) fusion

Deposition date:

2018-10-03

Original release date:

2018-11-14

Authors:

Ulmer, Tobias

Citation:

Citation: Bravo-Arredondo, Jose; Kegulian, Natalie; Schmidt, Thomas; Pandey, Nitin; Situ, Alan; Langen, Ralf; Ulmer, Tobias. "The folding equilibrium of huntingtin exon 1 monomer depends on its polyglutamine tract." J. Biol. Chem. 293, 19613-19623 (2018).
PubMed: 30315108

Assembly members:

Assembly members:
Thr-Httex1(Q7), polymer, 212 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET32a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Thr-Httex1(Q7): MSDKIIHLTDDSFDTDVLKA DGAILVDFWAEWSGPSKMIA PILDEIADEYQGKLTVAKLN IDQNPGTAPKYGIRGIPTLL LFKNGEVAATKVGALSKGQL KEFLDANLAGSGSGERQHMD SPDLGTDDDDKAMATLEKLM KAFESLKSFQQQQQQQPPPP PPPPPPPQLPQPPPQAQPLL PQPQPPPPPPPPPPGPAVAE EPLHRPHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	288
15N chemical shifts	154
1H chemical shifts	154

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	monomer	1

Entities:

Entity 1, monomer 212 residues - Formula weight is not available

1

MET

SER

ASP

LYS

ILE

HIS

LEU

THR

ASP

2

ASP

SER

PHE

ASP

THR

ASP

VAL

LEU

LYS

ALA

3

ASP

GLY

ALA

ILE

LEU

VAL

ASP

PHE

TRP

ALA

4

GLU

TRP

SER

GLY

PRO

SER

LYS

MET

ILE

ALA

5

PRO

ILE

LEU

ASP

GLU

ILE

ALA

ASP

GLU

TYR

6

GLN

GLY

LYS

LEU

THR

VAL

ALA

LYS

LEU

ASN

7

ILE

ASP

GLN

ASN

PRO

GLY

THR

ALA

PRO

LYS

8

TYR

GLY

ILE

ARG

GLY

ILE

PRO

THR

LEU

9

LEU

PHE

LYS

ASN

GLY

GLU

VAL

ALA

THR

10

LYS

VAL

GLY

ALA

LEU

SER

LYS

GLY

GLN

LEU

11

LYS

GLU

PHE

LEU

ASP

ALA

ASN

LEU

ALA

GLY

12

SER

GLY

SER

GLY

GLU

ARG

GLN

HIS

MET

ASP

13

SER

PRO

ASP

LEU

GLY

THR

ASP

14

LYS

ALA

MET

ALA

THR

LEU

GLU

LYS

LEU

MET

15

LYS

ALA

PHE

GLU

SER

LEU

LYS

SER

PHE

GLN

16

GLN

PRO

17

PRO

GLN

LEU

PRO

18

GLN

PRO

GLN

ALA

GLN

PRO

LEU

19

PRO

GLN

PRO

GLN

PRO

20

PRO

GLY

PRO

ALA

VAL

ALA

GLU

21

GLU

PRO

LEU

HIS

ARG

PRO

HIS

22

HIS

Samples:

sample_1: Thr-Httex1(Q7), [U-99% 13C; U-99% 15N], 0.3 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 6.0; pressure: ambient atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

Bruker Avance 700 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks